Analysis of the quality of crystallographic data and the limitations of structural models

J Gen Physiol. 2017 Dec 4;149(12):1091-1103. doi: 10.1085/jgp.201711852. Epub 2017 Oct 31.

Abstract

Crystal structures provide visual models of biological macromolecules, which are widely used to interpret data from functional studies and generate new mechanistic hypotheses. Because the quality of the collected x-ray diffraction data directly affects the reliability of the structural model, it is essential that the limitations of the models are carefully taken into account when making interpretations. Here we use the available crystal structures of members of the glutamate transporter family to illustrate the importance of inspecting the data that underlie the structural models. Crystal structures of glutamate transporters in multiple different conformations have been solved, but most structures were determined at relatively low resolution, with deposited models based on crystallographic data of moderate quality. We use these examples to demonstrate the extent to which mechanistic interpretations can be made safely.

Publication types

  • Review

MeSH terms

  • Amino Acid Transport System X-AG / chemistry*
  • Amino Acid Transport System X-AG / metabolism
  • Animals
  • Binding Sites
  • Crystallography, X-Ray / methods
  • Crystallography, X-Ray / standards*
  • Humans
  • Molecular Docking Simulation / standards*
  • Molecular Dynamics Simulation / standards*
  • Protein Binding

Substances

  • Amino Acid Transport System X-AG

Associated data

  • PDB/1XFH
  • PDB/2NWL
  • PDB/2NWX
  • PDB/2NWW
  • PDB/3KBC
  • PDB/3V8F
  • PDB/3V8G
  • PDB/4IZM
  • PDB/4KY0
  • PDB/4P6H
  • PDB/4P1A
  • PDB/4P19
  • PDB/4P3J
  • PDB/4OYE
  • PDB/4OYF
  • PDB/4OYG
  • PDB/5CFY
  • PDB/4X2S
  • PDB/5DWY
  • PDB/5E9S
  • PDB/5LLM
  • PDB/5LM4
  • PDB/5LLU
  • PDB/5MJU